1ww5: Difference between revisions

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 ==Agrocybe cylindracea galectin complexed with 3'-sulfonyl lactose==
-<StructureSection load='1ww5' size='340' side='right' caption='[[1ww5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='1ww5' size='340' side='right'caption='[[1ww5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ww5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrocybe_cylindracea Agrocybe cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WW5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ww5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrocybe_cylindracea Agrocybe cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WW5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=SGA:O3-SULFONYLGALACTOSE'>SGA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ww4|1ww4]], [[1ww6|1ww6]], [[1ww7|1ww7]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PRD_900068:lactose-3-sulfate'>PRD_900068</scene>, <scene name='pdbligand=SGA:O3-SULFONYLGALACTOSE'>SGA</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ww5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ww5 OCA], [http://pdbe.org/1ww5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ww5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ww5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ww5 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ww5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ww5 OCA], [https://pdbe.org/1ww5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ww5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ww5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ww5 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATLE_CYCAE ATLE_CYCAE] Anti-tumor lectin with DNase activity. Inhibits the growth of several tumor cell lines in vitro. Induces lymphocyte infiltration and necrosis of tumor cells in a mouse tumor model. Induces apoptosis in HeLa cells. Binds N-acetylneuraminyl lactose (N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucose) (PubMed:16051274).<ref>PMID:12757412</ref> <ref>PMID:16051274</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 20: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ww5 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Galectin from an edible fungus Agrocybe cylindracea (ACG) has a strong preference for N-acetylneuraminyl lactose (NeuAcalpha2-3lactose). The sugar recognition mechanism of ACG was explored by the X-ray crystallographic analyses of ligand-free ACG, and its complex with lactose, 3'-sulfonyl lactose and NeuAcalpha2-3lactose. The refined structure shows that ACG is a "proto"-type galectin composed of a beta-sandwich of two antiparallel sheets, each with six strands, in contrast to the five and six strands in animal galectins. ACG dimer in solution was classified as being among the "layer"-type. The carbohydrate recognition domain (CRD) of this galectin is common to those of animal galectins, except for substitution of one residue, Ala64, which corresponds to Asn46 in human galectin 1. A five-residue insertion in ACG at positions 42-46 involving Ser44 and Asn46 modified the architecture of the sugar binding site that contributes sialic acid specificity. Furthermore, it was found that the binding of a sulfate ion near the CRD in the ligand-free form led to a change in the conformation of the loop region caused by main-chain cis/trans transition between Ser44 and Pro45.
-Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate.,Ban M, Yoon HJ, Demirkan E, Utsumi S, Mikami B, Yagi F J Mol Biol. 2005 Aug 26;351(4):695-706. PMID:16051274<ref>PMID:16051274</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ww5" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Galectin|Galectin]]
+*[[Galectin 3D structures|Galectin 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 28: @@
 </StructureSection>
 [[Category: Agrocybe cylindracea]]
-[[Category: Ban, M]]
+[[Category: Large Structures]]
-[[Category: Demirkan, E]]
+[[Category: Ban M]]
-[[Category: Mikami, B]]
+[[Category: Demirkan E]]
-[[Category: Utsumi, S]]
+[[Category: Mikami B]]
-[[Category: Yagi, F]]
+[[Category: Utsumi S]]
-[[Category: Yoon, H J]]
+[[Category: Yagi F]]
-[[Category: 3'-sulfated lactose]]
+[[Category: Yoon HJ]]
-[[Category: Agrocybe cylindracea galectin]]
-[[Category: Carbohydrate recognition domain]]
-[[Category: Fungal galectin]]
-[[Category: Sugar binding protein]]
-[[Category: X-ray crystallographic analysis]]